CIP1_HUMAN
ID CIP1_HUMAN Reviewed; 277 AA.
AC Q9NPC3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=E3 ubiquitin-protein ligase CCNB1IP1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12612082};
DE AltName: Full=Cyclin-B1-interacting protein 1;
DE AltName: Full=Human enhancer of invasion 10;
DE AltName: Full=RING-type E3 ubiquitin transferase CCNB1IP1 {ECO:0000305};
GN Name=CCNB1IP1; Synonyms=C14orf18, HEI10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-28; HIS-30 AND CYS-33,
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND CCNB1,
RP UBIQUITINATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12612082; DOI=10.1128/mcb.23.6.2109-2122.2003;
RA Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
RT "A novel RING finger protein, human enhancer of invasion 10, alters mitotic
RT progression through regulation of cyclin B levels.";
RL Mol. Cell. Biol. 23:2109-2122(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH NF2.
RX PubMed=16532029; DOI=10.1038/sj.onc.1209475;
RA Gronholm M., Muranen T., Toby G.G., Utermark T., Hanemann C.O.,
RA Golemis E.A., Carpen O.;
RT "A functional association between merlin and HEI10, a cell cycle
RT regulator.";
RL Oncogene 25:4389-4398(2006).
RN [7]
RP FUNCTION.
RX PubMed=17297447; DOI=10.1038/sj.onc.1210282;
RA Singh M.K., Nicolas E., Gherraby W., Dadke D., Lessin S., Golemis E.A.;
RT "HEI10 negatively regulates cell invasion by inhibiting cyclin B/Cdk1 and
RT other promotility proteins.";
RL Oncogene 26:4825-4832(2007).
CC -!- FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for
CC crossing-over during meiosis: required during zygonema to limit the
CC colocalization of RNF212 with MutS-gamma-associated recombination sites
CC and thereby establish early differentiation of crossover and non-
CC crossover sites. Later, it is directed by MutL-gamma to stably
CC accumulate at designated crossover sites. Probably promotes the
CC dissociation of RNF212 and MutS-gamma to allow the progression of
CC recombination and the implementation of the final steps of crossing
CC over (By similarity). Modulates cyclin-B levels and participates in the
CC regulation of cell cycle progression through the G2 phase.
CC Overexpression causes delayed entry into mitosis. {ECO:0000250,
CC ECO:0000269|PubMed:12612082, ECO:0000269|PubMed:17297447}.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Modulates cyclin B levels and
CC participates in the regulation of cell cycle progression through the G2
CC phase. Overexpression causes delayed entry into mitosis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:12612082};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CCNB1, UBE2L3 and NF2.
CC {ECO:0000269|PubMed:12612082, ECO:0000269|PubMed:16532029}.
CC -!- INTERACTION:
CC Q9NPC3; P54253: ATXN1; NbExp=6; IntAct=EBI-745269, EBI-930964;
CC Q9NPC3; P14635: CCNB1; NbExp=2; IntAct=EBI-745269, EBI-495332;
CC Q9NPC3; Q9NPC3: CCNB1IP1; NbExp=3; IntAct=EBI-745269, EBI-745269;
CC Q9NPC3; Q93034: CUL5; NbExp=3; IntAct=EBI-745269, EBI-1057139;
CC Q9NPC3; Q7L775: EPM2AIP1; NbExp=4; IntAct=EBI-745269, EBI-6255981;
CC Q9NPC3; P42858: HTT; NbExp=6; IntAct=EBI-745269, EBI-466029;
CC Q9NPC3; Q14145: KEAP1; NbExp=4; IntAct=EBI-745269, EBI-751001;
CC Q9NPC3; P19012: KRT15; NbExp=4; IntAct=EBI-745269, EBI-739566;
CC Q9NPC3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-745269, EBI-741158;
CC Q9NPC3; P54646: PRKAA2; NbExp=4; IntAct=EBI-745269, EBI-1383852;
CC Q9NPC3; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-745269, EBI-745392;
CC Q9NPC3; P62972; Xeno; NbExp=2; IntAct=EBI-745269, EBI-412964;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the
CC synaptonemal complex.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart. Detected at intermediate
CC levels in liver and kidney, and at low levels in placenta, brain and
CC lung. {ECO:0000269|PubMed:12612082}.
CC -!- PTM: Ubiquitinated; autoubiquitinated. {ECO:0000269|PubMed:12612082}.
CC -!- PTM: Phosphorylated by CDK1 on serine or threonine residues (in vitro).
CC {ECO:0000269|PubMed:12612082}.
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DR EMBL; AF216381; AAF36386.1; -; mRNA.
DR EMBL; AL161994; CAB82326.1; -; mRNA.
DR EMBL; AK026233; BAB15403.1; -; mRNA.
DR EMBL; BX161423; CAD61896.1; -; mRNA.
DR EMBL; BX161424; CAD61897.1; -; mRNA.
DR EMBL; BX247978; CAD62312.1; -; mRNA.
DR EMBL; BC000369; AAH00369.1; -; mRNA.
DR EMBL; BC001218; AAH01218.1; -; mRNA.
DR EMBL; BC004435; AAH04435.1; -; mRNA.
DR CCDS; CCDS9547.1; -.
DR PIR; T47153; T47153.
DR RefSeq; NP_067001.3; NM_021178.4.
DR RefSeq; NP_878269.1; NM_182849.2.
DR RefSeq; NP_878272.1; NM_182852.3.
DR AlphaFoldDB; Q9NPC3; -.
DR SMR; Q9NPC3; -.
DR BioGRID; 121779; 21.
DR IntAct; Q9NPC3; 14.
DR STRING; 9606.ENSP00000409896; -.
DR GlyGen; Q9NPC3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPC3; -.
DR PhosphoSitePlus; Q9NPC3; -.
DR BioMuta; CCNB1IP1; -.
DR DMDM; 37078756; -.
DR MassIVE; Q9NPC3; -.
DR PaxDb; Q9NPC3; -.
DR PeptideAtlas; Q9NPC3; -.
DR PRIDE; Q9NPC3; -.
DR ProteomicsDB; 81965; -.
DR Antibodypedia; 22006; 231 antibodies from 26 providers.
DR DNASU; 57820; -.
DR Ensembl; ENST00000353689.8; ENSP00000337396.4; ENSG00000100814.18.
DR Ensembl; ENST00000358932.9; ENSP00000351810.4; ENSG00000100814.18.
DR Ensembl; ENST00000398160.6; ENSP00000381226.2; ENSG00000100814.18.
DR Ensembl; ENST00000398163.6; ENSP00000381229.2; ENSG00000100814.18.
DR Ensembl; ENST00000398169.7; ENSP00000381235.3; ENSG00000100814.18.
DR Ensembl; ENST00000437553.6; ENSP00000409896.2; ENSG00000100814.18.
DR GeneID; 57820; -.
DR KEGG; hsa:57820; -.
DR MANE-Select; ENST00000358932.9; ENSP00000351810.4; NM_021178.5; NP_067001.3.
DR UCSC; uc001vwv.5; human.
DR CTD; 57820; -.
DR DisGeNET; 57820; -.
DR GeneCards; CCNB1IP1; -.
DR HGNC; HGNC:19437; CCNB1IP1.
DR HPA; ENSG00000100814; Low tissue specificity.
DR MIM; 608249; gene.
DR neXtProt; NX_Q9NPC3; -.
DR OpenTargets; ENSG00000100814; -.
DR PharmGKB; PA134863884; -.
DR VEuPathDB; HostDB:ENSG00000100814; -.
DR eggNOG; ENOG502RMFV; Eukaryota.
DR GeneTree; ENSGT00390000002849; -.
DR HOGENOM; CLU_049340_3_0_1; -.
DR InParanoid; Q9NPC3; -.
DR OMA; HQERMYQ; -.
DR OrthoDB; 1383870at2759; -.
DR PhylomeDB; Q9NPC3; -.
DR TreeFam; TF328863; -.
DR PathwayCommons; Q9NPC3; -.
DR SignaLink; Q9NPC3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57820; 14 hits in 1116 CRISPR screens.
DR ChiTaRS; CCNB1IP1; human.
DR GeneWiki; CCNB1IP1; -.
DR GenomeRNAi; 57820; -.
DR Pharos; Q9NPC3; Tbio.
DR PRO; PR:Q9NPC3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9NPC3; protein.
DR Bgee; ENSG00000100814; Expressed in left ovary and 201 other tissues.
DR ExpressionAtlas; Q9NPC3; baseline and differential.
DR Genevisible; Q9NPC3; HS.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0051026; P:chiasma assembly; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR InterPro; IPR042448; CCNB1IP1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR14305; PTHR14305; 1.
DR Pfam; PF14634; zf-RING_5; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Meiosis; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..277
FT /note="E3 ubiquitin-protein ligase CCNB1IP1"
FT /id="PRO_0000055874"
FT ZN_FING 4..51
FT /note="RING-type; atypical"
FT COILED 127..182
FT /evidence="ECO:0000255"
FT MUTAGEN 28
FT /note="C->A: Abrogates induction of filamentous growth in
FT yeast; when associated with A-30 and A-33."
FT /evidence="ECO:0000269|PubMed:12612082"
FT MUTAGEN 30
FT /note="H->A: Abrogates induction of filamentous growth in
FT yeast; when associated with A-28 and A-33."
FT /evidence="ECO:0000269|PubMed:12612082"
FT MUTAGEN 33
FT /note="C->A: Abrogates induction of filamentous growth in
FT yeast; when associated with A-28 and A-30."
FT /evidence="ECO:0000269|PubMed:12612082"
SQ SEQUENCE 277 AA; 31544 MW; 885723B01A35225A CRC64;
MSLCEDMLLC NYRKCRIKLS GYAWVTACSH IFCDQHGSGE FSRSPAICPA CNSTLSGKLD
IVRTELSPSE EYKAMVLAGL RPEIVLDISS RALAFWTYQV HQERLYQEYN FSKAEGHLKQ
MEKIYTQQIQ SKDVELTSMK GEVTSMKKVL EEYKKKFSDI SEKLMERNRQ YQKLQGLYDS
LRLRNITIAN HEGTLEPSMI AQSGVLGFPL GNNSKFPLDN TPVRNRGDGD GDFQFRPFFA
GSPTAPEPSN SFFSFVSPSR ELEQQQVSSR AFKVKRI
